ID   PLC12_CAEEL             Reviewed;         391 AA.
AC   Q11087;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 39.
DE   RecName: Full=Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase acl-12;
DE            Short=1-AGP acyltransferase;
DE            Short=1-AGPAT;
DE            EC=2.3.1.51;
DE   AltName: Full=Lysophosphatidic acid acyltransferase;
DE            Short=LPAAT;
GN   Name=acl-12; ORFNames=C01C10.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic
CC       acid by incorporating an acyl moiety at the sn-2 position of the
CC       glycerol backbone (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate =
CC       CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC       CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity
CC       and may constitute the binding site for the phosphate moiety of
CC       the glycerol-3-phosphate (By similarity).
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family.
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DR   EMBL; U23526; AAB36850.1; -; Genomic_DNA.
DR   PIR; T15366; T15366.
DR   RefSeq; NP_509260.1; -.
DR   UniGene; Cel.7660; -.
DR   Ensembl; C01C10.3; Caenorhabditis elegans.
DR   GeneID; 181001; -.
DR   KEGG; cel:C01C10.3; -.
DR   NMPDR; fig|6239.3.peg.23768; -.
DR   WormBase; WBGene00015295; acl-12.
DR   WormPep; C01C10.3; CE02449.
DR   OMA; Q11087; WVIYNIW.
DR   BRENDA; 2.3.1.51; 672.
DR   NextBio; 911926; -.
DR   ArrayExpress; Q11087; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferas...; IEA:EC.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002123; Acyltransferase.
DR   SMART; SM00563; PlsC; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Complete proteome; Membrane;
KW   Phospholipid biosynthesis; Transferase; Transmembrane.
FT   CHAIN         1    391       Putative 1-acyl-sn-glycerol-3-phosphate
FT                                acyltransferase acl-12.
FT                                /FTId=PRO_0000065097.
FT   TRANSMEM     47     67       Potential.
FT   TRANSMEM     84    104       Potential.
FT   MOTIF       124    129       HXXXXD motif.
SQ   SEQUENCE   391 AA;  44718 MW;  FB5C062A0172A8C1 CRC64;
     MLKSGLMDTD DQKVGVRVAN IDMSERTDNV HLIEIRRIIS LVGAAYFFFM TAWVVPVACV
     ITVSLLFPLM LFSTPLFNYL EHKLCAMVNA HWNAVSVFVG ATVTEYGTNL AGYAEEKCLL
     LANHLGLLDH FVLMQSLNGK GSIRSRWMWV IYNIWKYTPL GVMWTSHGNF FVNGGVSKRD
     SVLSSFRDHL KNSFYKYDYG WVIMYPEGSR LYLVKNSGRT FAEKNGLKPL DNCVYPRTGA
     AHAVLDVLGP TDDSLSMSKC GKGEPIKYII DATIGYRKGA VPDICDVMMG DWESVEASQF
     AVHYDVIPVK PEWSDENLLK EFLYERYIIK DKLLAEFYKT GHFPGDKTKV IPNNYEMMFA
     QVFWGCLYYA HYVYWLRPLI VHSWTSFLSI F
//